SASDC39 – Human Rev7 dimer in complex with Rev3 peptide @ 9.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.0 nm
Dmax 11.4 nm
VolumePorod 107 nm3

SASDC49 – Human Rev7 dimer in complex with Rev3 peptide @ 6.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 105 nm3

SASDC59 – Human Rev7 dimer in complex with Rev3 peptide @ 7.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.1 nm
VolumePorod 106 nm3

SASDC69 – Human Rev7 dimer in complex with Rev3 peptide @ 4.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm

SASDC79 – Human Rev7 dimer in complex with Rev3 peptide @ 3.0mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC89 – Human Rev7 dimer in complex with Rev3 peptide @ 1.5 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.7 nm

SASDEM3 – Dimeric class D beta-lactamase OXA-48

Beta-lactamase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-lactamase dimer, 56 kDa Klebsiella pneumoniae protein
Buffer: 50 mM HEPES 50 mM K2SO4, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 23
The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity. FEBS J (2018)
Lund BA, Thomassen AM, Nesheim BHB, Carlsen TJO, Isaksson J, Christopeit T, Leiros HS
RgGuinier 2.5 nm
Dmax 7.4 nm
VolumePorod 74 nm3

SASDD62 – Microtubule associated protein MAP2c (isoform 3); 12 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 8.3 nm

SASDD72 – Microtubule associated protein MAP2c (isoform 3); 6 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 7.9 nm

SASDD82 – Microtubule associated protein MAP2c (isoform 3); 3 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 6.9 nm

4722 hits found.